Gluten, major histocompatibility complex, and the small intestine

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Structure of the human class I histocompatibility antigen, HLA-A2.

P J Bjorkman, M Saper, B Samraoui … (1987)

The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.

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Empirical predictions of protein conformation.

P. Chou, G D Fasman (1978)

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The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens.

P J Bjorkman, M Saper, B Samraoui … (1987)

Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.